The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Roles of electrostatic interaction in proteins
Abstract
Electrostatic effects play an essential role in specific molecular recognition and molecular assembly in many biologically important molecules. The specific electric field at the active site also regulates the catalytic reaction of a protein. Moreover, intramolecular or inter-subunit electrostatic interactions, such as saltbridges, hydrogen bonds, and charge-dipole interactions, are considered to work to stabilize protein molecules. Those electrostatic roles recently observed in proteins are reviewed with a description of the origins and principles of electrostatic forces, and analyses will be made using simple models to illuminate the physical basis.
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Cites
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Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a001 · Cited by 2,172
Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914
A new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Origins and evolutionary relationships of retroviruses
Doolittle, R. F., Johnson, M. S., & McClure, M. A. (1989) · The Quarterly Review of Biology · doi:10.1086/416128 · Cited by 577
Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
Davies, J. F., Hostomska, Z., Hostomsky, Z., Jordan, S. R., & Matthews, D. A. (1991) · Science · doi:10.1126/science.1707186 · Cited by 570
Three-dimensional structure of ribonuclease H from E. coli
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Recombining the structures of HIV integrase, RuvC and RNase H
Yang, W., & Steitz, T. A. (1995) · Structure · doi:10.1016/s0969-2126(01)00142-3 · Cited by 246
How does RNase H recognize a DNA.RNA hybrid?
Nakamura, H., Oda, Y., Iwai, S., Inoue, H., Ohtsuka, E., Kanaya, S., Kimura, S., Katsuda, C., Katayanagi, K., & Morikawa, K. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.24.11535 · Cited by 193
Self-citationKanaya, S., Kohara, A., Miura, Y., Sekiguchi, A., Iwai, S., Inoue, H., Ohtsuka, E., & Ikehara, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39607-3 · Cited by 180
Cited by
Russell, R. J. M., Ferguson, J. M. C., Hough, D. W., Danson, M. J., & Taylor, G. L. (1997) · Biochemistry · doi:10.1021/bi9705321 · Cited by 275
AlphaFold, allosteric, and orthosteric drug discovery: Ways forward
Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103551 · Cited by 96
Wang, B., Lei, X., Tian, W., Perez-Rathke, A., Tseng, Y.-Y., & Liang, J. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad206 · Cited by 11
(2024) · doi:10.1002/sstr.202400086 · Cited by 4
Metadata
- Authors
- Nakamura, H.
- Venue
- Quarterly Reviews of Biophysics
- Publisher
- Cambridge University Press (CUP)
- Published
- 1996-02
- Volume
- 29
- Issue
- 1
- Pages
- 1-90
- ISSN
- 0033-5835 (ISSN-L)
- 1469-8994
- OpenAlex
- W2160988970
- Cited by
- 306
- References
- 10
- FWCI
- 1.40
- Type
- journal article
- Language
- en
- Open access
- closed
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
